Literature DB >> 1816370

Cross-bridge movement in fast and slow skeletal muscles of the chick.

I Matsubara1, N Yagi, Y Saeki, S Kurihara.   

Abstract

1. Fast (posterior latissimus dorsi, PLD) and slow (anterior latissimus dorsi, ALD) muscles of the chick were studied by time-resolved X-ray diffraction using a synchrotron radiation source. 2. In both muscles and at both 20 and 30 degrees C, intensities of the X-ray equatorial reflections changed faster than tension at the beginning of tetanus. When the intensity change was converted into the mass transfer from the thick to the thin filament, the difference between the half-rise times of the transfer and tension development at 20 degrees C was 140 ms in ALD and 37 ms in PLD. At 30 degrees C it was 110 ms and 10-20 ms for ALD and PLD respectively. 3. These results indicate that in the early stage of contraction, some of the myosin heads in the vicinity of the thin filament are developing little or no tension, and suggest that the fast and slow muscles differ in the transition rate of myosin heads from the state of attachment with low tension to that with high tension.

Entities:  

Mesh:

Substances:

Year:  1991        PMID: 1816370      PMCID: PMC1180188          DOI: 10.1113/jphysiol.1991.sp018741

Source DB:  PubMed          Journal:  J Physiol        ISSN: 0022-3751            Impact factor:   5.182


  19 in total

1.  Muscle structure and theories of contraction.

Authors:  A F HUXLEY
Journal:  Prog Biophys Biophys Chem       Date:  1957

2.  Weakly attached cross-bridges in relaxed frog muscle fibers.

Authors:  D W Jung; T Blangé; H de Graaf; B W Treijtel
Journal:  Biophys J       Date:  1989-04       Impact factor: 4.033

3.  Stiffness of skinned rabbit psoas fibers in MgATP and MgPPi solution.

Authors:  B Brenner; J M Chalovich; L E Greene; E Eisenberg; M Schoenberg
Journal:  Biophys J       Date:  1986-10       Impact factor: 4.033

4.  Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction.

Authors:  M Kress; H E Huxley; A R Faruqi; J Hendrix
Journal:  J Mol Biol       Date:  1986-04-05       Impact factor: 5.469

5.  X-ray evidence for radial cross-bridge movement and for the sliding filament model in actively contracting skeletal muscle.

Authors:  J C Haselgrove; H E Huxley
Journal:  J Mol Biol       Date:  1973-07-15       Impact factor: 5.469

6.  X-ray diffraction studies of the structural state of crossbridges in skinned frog sartorius muscle at low ionic strength.

Authors:  S G Xu; M Kress; H E Huxley
Journal:  J Muscle Res Cell Motil       Date:  1987-02       Impact factor: 2.698

7.  Time-resolved x-ray diffraction studies on the intensity changes of the 5.9 and 5.1 nm actin layer lines from frog skeletal muscle during an isometric tetanus using synchrotron radiation.

Authors:  K Wakabayashi; H Tanaka; Y Amemiya; A Fujishima; T Kobayashi; T Hamanaka; H Sugi; T Mitsui
Journal:  Biophys J       Date:  1985-06       Impact factor: 4.033

8.  The rate-limiting step in the actomyosin adenosinetriphosphatase cycle.

Authors:  L A Stein; P B Chock; E Eisenberg
Journal:  Biochemistry       Date:  1984-03-27       Impact factor: 3.162

9.  Intensification of the 5.9-nm actin layer line in contracting muscle.

Authors:  I Matsubara; N Yagi; H Miura; M Ozeki; T Izumi
Journal:  Nature       Date:  1984 Nov 29-Dec 5       Impact factor: 49.962

10.  X-ray diffraction evidence for cross-bridge formation in relaxed muscle fibers at various ionic strengths.

Authors:  B Brenner; L C Yu; R J Podolsky
Journal:  Biophys J       Date:  1984-09       Impact factor: 4.033

View more
  2 in total

1.  Cross-bridge movement in rat slow skeletal muscle as a function of calcium concentration.

Authors:  H Honda; Y Koiwa; N Yagi; I Matsubara
Journal:  Pflugers Arch       Date:  1996-09       Impact factor: 3.657

2.  Lattice arrangement of myosin filaments correlates with fiber type in rat skeletal muscle.

Authors:  Weikang Ma; Kyoung Hwan Lee; Shixin Yang; Thomas C Irving; Roger Craig
Journal:  J Gen Physiol       Date:  2019-11-07       Impact factor: 4.086

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.